A model of alpha-helical distribution in proteins.
It is shown that alpha-helical content of eleven proteins is well correlated with alanine plus leucine content. These residues, taken singly or together, are to a first approximation randomly distributed in the four proteins whose tertiary structures have been determined (i.e., myoglobin, lysozyme, ribonuclease, alpha-chymotrypsin). A model based on the concept that certain randomly distributed residues specifically participate in helix nucleation is shown to be in reasonable agreement with the presently published structures.
D000409:Alanine; D000595:Amino Acid Sequence; D002918:Chymotrypsin; D005971:Glutamates; D006454:Hemoglobins; D007930:Leucine; D008956:Models, Chemical; D009113:Muramidase; D009211:Myoglobin; D011506:Proteins; D012260:Ribonucleases; D014633:Valine
D005971:Glutamates; D006454:Hemoglobins; D009211:Myoglobin; D011506:Proteins; D012260:Ribonucleases; D009113:Muramidase; D002918:Chymotrypsin; D007930:Leucine; D014633:Valine; D000409:Alanine